The cruciform DNA‐binding protein Crp1 stimulates the endonuclease activity of Mus81–Mms4 in Saccharomyces cerevisiae

FEBS Letters ◽  
2020 ◽  
Vol 594 (24) ◽  
pp. 4320-4337
Author(s):  
Huong Thi Thu Phung ◽  
Diem Hong Tran ◽  
Ta Xuan Nguyen
1992 ◽  
Vol 11 (10) ◽  
pp. 3787-3796 ◽  
Author(s):  
S. Zhang ◽  
C. Lockshin ◽  
A. Herbert ◽  
E. Winter ◽  
A. Rich

Chromosoma ◽  
1993 ◽  
Vol 102 (5) ◽  
pp. 348-354 ◽  
Author(s):  
H. Kotani ◽  
E. B. Kmiec ◽  
W. K. Holloman

Biochemistry ◽  
1994 ◽  
Vol 33 (47) ◽  
pp. 14185-14196 ◽  
Author(s):  
Christopher E. Pearson ◽  
Marcia T. Ruiz ◽  
Gerald B. Price ◽  
Maria Zannis-Hadjopoulos

1995 ◽  
Vol 15 (11) ◽  
pp. 5929-5936 ◽  
Author(s):  
S W Jeong ◽  
W H Lang ◽  
R H Reeder

The Saccharomyces cerevisiae polymerase I (polI) transcription terminator utilizes a DNA-binding protein (Reb1p) as part of a signal that causes the polymerase to pause prior to release from the template. To study the release element of the terminator, independent of the Reb1p pause signal, we have replaced the Reb1p binding site with the binding site for the lac repressor, which acts as a self-contained heterologous pause signal for polI. Release efficiency is maximal when the lac repressor causes polI to pause in exactly the same position that Reb1p would have caused it to pause, suggesting that polI must be precisely positioned for transcript release to occur. Mutational analysis shows that the release element is a region rich in T residues which codes for the extreme 3' end of the transcript and which has no apparent ability to form hairpins when transcribed into RNA. We discuss possible mechanisms whereby this polI release element might function.


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